2015
Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin
Farr GA, Hull M, Stoops EH, Bateson R, Caplan MJ. Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin. Molecular Biology Of The Cell 2015, 26: 4401-4411. PMID: 26424804, PMCID: PMC4666135, DOI: 10.1091/mbc.e14-09-1385.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkPlasma membraneE-cadherinK-ATPasePolarized MDCK epithelial cellsPost-Golgi traffickingCell surfacePolarized epithelial cellsEpithelial cellsMDCK epithelial cellsDistinct trafficking routesBiosynthetic traffickingCarrier vesiclesSecretory pathwayMembrane proteinsSurface deliveryBasolateral domainMost proteinsTrafficking routesGolgi complexTemperature blockTraffickingProteinMembraneCells
2010
Polycystin-1 Surface Localization Is Stimulated by Polycystin-2 and Cleavage at the G Protein-coupled Receptor Proteolytic Site
Chapin HC, Rajendran V, Caplan MJ. Polycystin-1 Surface Localization Is Stimulated by Polycystin-2 and Cleavage at the G Protein-coupled Receptor Proteolytic Site. Molecular Biology Of The Cell 2010, 21: 4338-4348. PMID: 20980620, PMCID: PMC3002387, DOI: 10.1091/mbc.e10-05-0407.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell MembraneCiliaFluorescent Antibody TechniqueHEK293 CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMutationPolycystic Kidney, Autosomal DominantProtein BindingProtein IsoformsProtein Processing, Post-TranslationalProtein Structure, TertiaryProtein TransportSwineTRPP Cation ChannelsConceptsG-protein-coupled receptor proteolytic siteGPS cleavagePC2 channel activitySurface deliveryChannel activityProteolytic siteSurface localizationPlasma membrane localizationC-terminal tailHuman embryonic kidney 293 cellsEmbryonic kidney 293 cellsPC2 mutationsKidney 293 cellsMembrane localizationSecretory pathwayMembrane proteinsBinding partnerTerminal tailPolycystin-2Effect of PC2Plasma membraneCiliary membraneTRP familyLLC-PK cellsCation channels
2009
Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells
Farr GA, Hull M, Mellman I, Caplan MJ. Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells. Journal Of Cell Biology 2009, 186: 269-282. PMID: 19620635, PMCID: PMC2717640, DOI: 10.1083/jcb.200901021.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCadherinsCell LineCell MembraneCell PolarityDogsEndosomesEpithelial CellsExocytosisGolgi ApparatusHumansMembrane GlycoproteinsMembrane ProteinsModels, MolecularProtein Structure, SecondaryProtein TransportReceptors, TransferrinRecombinant Fusion ProteinsSodium-Potassium-Exchanging ATPaseStaining and LabelingTrans-Golgi NetworkViral Envelope ProteinsConceptsBasolateral proteinsMembrane proteinsSurface deliveryK-ATPaseVesicular stomatitis virus G proteinPolarized epithelial cellsBasolateral membrane proteinsEpithelial cellsVirus G proteinBasolateral cell surfaceBasolateral deliveryTransport intermediatesGolgi networkSmall GTPasesPlasma membraneG proteinsCell surfaceProteinMultiple pathwaysBasolateral membraneGolgiPathwayCellsMembraneGTPases
2000
The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*
McCarthy J, Lim S, Elkind N, Trimmer J, Duvoisin R, Rodriguez-Boulan E, Caplan M. The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*. Journal Of Biological Chemistry 2000, 276: 9133-9140. PMID: 11106656, DOI: 10.1074/jbc.m008290200.Peer-Reviewed Original ResearchConceptsPolarized targetingCytoplasmic tailIntracellular compartmentsMadin-Darby canine kidney epithelial cellsVesicular stomatitis virus G proteinComplex neuronal functionMDCK cellsCell surface deliveryC-terminal tailCanine kidney epithelial cellsCytoplasmic tail domainVirus G proteinKidney epithelial cellsEntire cell surfaceCell surface expressionCytoplasmic domainTransmembrane portionSurface deliveryTail domainSynaptic microdomainsHuman placental alkaline phosphataseNeuronal polarizationMolecular signalsG proteinsCultured hippocampal neuronsThe Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*
Asano S, Kawada K, Kimura T, Grishin A, Caplan M, Takeguchi N. The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*. Journal Of Biological Chemistry 2000, 275: 8324-8330. PMID: 10722662, DOI: 10.1074/jbc.275.12.8324.Peer-Reviewed Original ResearchConceptsAlpha/beta assemblyN-glycosylation sitesATPase activityBeta assemblyPutative N-glycosylation sitesCarbohydrate chainsAlpha/beta complexSingle carbohydrate chainCatalytic subunitSurface deliveryFunctional enzymeAsparagine residuesAlpha subunitΒ-subunitBeta complexDelivery mechanismFunctional expressionComplete lossATPaseAssemblyExpressionSubunits
1997
Sorting and trafficking of ion transport proteins in polarized epithelial cells
Muth T, Dunbar L, Cortois-Coutry N, Roush D, Caplan M. Sorting and trafficking of ion transport proteins in polarized epithelial cells. Current Opinion In Nephrology & Hypertension 1997, 6: 455-459. PMID: 9327204, DOI: 10.1097/00041552-199709000-00008.Peer-Reviewed Original Research
1996
Real-time detection of the surface delivery of newly synthesized membrane proteins.
Andreose JS, Fumagalli G, Sigworth FJ, Caplan MJ. Real-time detection of the surface delivery of newly synthesized membrane proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 7661-7666. PMID: 8755532, PMCID: PMC38803, DOI: 10.1073/pnas.93.15.7661.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBungarotoxinsCell LineCell MembraneElectrophysiologyFourier AnalysisGolgi ApparatusGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateIon ChannelsKineticsMembrane PotentialsMembrane ProteinsMiceMuscle, SkeletalProtein Processing, Post-TranslationalReceptors, NicotinicTime FactorsConceptsMembrane proteinsPlasma membraneCell surfaceDegrees C temperature blockCultured muscle cellsConstitutive trafficTransport vesiclesConstitutive deliveryFusion eventsSurface deliveryFusion poreExocytotic vesiclesAChR moleculeGolgi complexTemperature blockAChR proteinNicotinic acetylcholine receptorsIon channel propertiesMost cellsVesiclesProteinCurrent fluctuationsMuscle cellsAcetylcholine receptorsGuanosine 5'
1993
Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly
Gottardi CJ, Caplan MJ. Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly. Journal Of Biological Chemistry 1993, 268: 14342-14347. PMID: 8390991, DOI: 10.1016/s0021-9258(19)85246-8.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitK-ATPase beta subunitAlpha subunitBeta subunitCell surface expressionTerminal halfK-ATPaseCell surface deliveryEfficient cell surface expressionK-ATPase alphaNH2-terminal halfCOS-1 cellsIon-transporting ATPasesProtein domainsK-ATPase enzymeSubunit assemblySurface deliveryIntracellular vesiclesSubunit chimerasIndividual subunitsActive enzymeMolecular requirementsSubunitsCell surfaceBeta protein
1986
Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes
Caplan M, Anderson H, Palade G, Jamieson J. Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes. Cell 1986, 46: 623-631. PMID: 3015421, DOI: 10.1016/0092-8674(86)90888-3.Peer-Reviewed Original ResearchConceptsBasolateral plasmalemmal domainsPlasmalemmal domainsNative proteinCell surface deliveryMadin-Darby canine kidney cellsBasolateral plasma membraneBasolateral cell surfacePulse labeling experimentsCanine kidney cellsIntracellular sortingProper sortingSurface deliveryPlasma membraneAcidic compartmentsDarby canine kidney cellsCell surfaceApical surfaceKidney cellsLabeling experimentsTwo-chamber culture systemProteinSortingCulture system